When a polypeptide is in its native conformation, there are weak interactions between its R groups. However, when it is denatured there are similar interactions between the protein groups and water. What then accounts for the greater stability of the native conformation?

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When a polypeptide is in its native conformation, there are weak interactions between its R groups. However, when it is denatured there are similar interactions between the protein groups and water. What then accounts for the greater stability of the native conformation?

Chemistry
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I guess it depends what the R groups are. I'm assuming they're non-polar since they have a greater stability in the proteins native conformation (which is likely a globular structure shielding the R groups from water).

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